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P10968 (AGI1_WHEAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Agglutinin isolectin 1
Alternative name(s):
Isolectin A
WGA1
OrganismTriticum aestivum (Wheat) [Complete proteome]
Taxonomic identifier4565 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladePooideaeTriticeaeTriticum

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin.

Subunit structure

Homodimer, u-shaped.

Miscellaneous

The 4 sites proposed for binding to carbohydrates (N-acetyl-D-glucosamine) of receptor molecules are on the surface of the agglutinin molecule.

Sequence similarities

Contains 4 chitin-binding type-1 domains.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2
Chain27 – 197171Agglutinin isolectin 1
PRO_0000005255
Propeptide198 – 21215
PRO_0000005256

Regions

Domain27 – 6842Chitin-binding type-1 1
Domain69 – 11143Chitin-binding type-1 2
Domain112 – 15443Chitin-binding type-1 3
Domain155 – 19743Chitin-binding type-1 4
Region36 – 383Substrate binding
Region88 – 9912Substrate binding
Region140 – 1412Substrate binding

Amino acid modifications

Modified residue271Pyrrolidone carboxylic acid
Disulfide bond29 ↔ 44
Disulfide bond38 ↔ 50
Disulfide bond43 ↔ 57
Disulfide bond61 ↔ 66
Disulfide bond72 ↔ 87
Disulfide bond81 ↔ 93
Disulfide bond86 ↔ 100
Disulfide bond104 ↔ 109
Disulfide bond115 ↔ 130
Disulfide bond124 ↔ 136
Disulfide bond129 ↔ 143
Disulfide bond147 ↔ 152
Disulfide bond158 ↔ 173
Disulfide bond167 ↔ 179
Disulfide bond172 ↔ 186
Disulfide bond190 ↔ 195

Experimental info

Sequence conflict631N → D AA sequence Ref.2

Secondary structure

...................................... 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10968 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: EC7B6F007DDC15EB

FASTA21221,239
        10         20         30         40         50         60 
MKMMSTRALA LGAAAVLAFA AATAQAQRCG EQGSNMECPN NLCCSQYGYC GMGGDYCGKG 

        70         80         90        100        110        120 
CQNGACWTSK RCGSQAGGAT CTNNQCCSQY GYCGFGAEYC GAGCQGGPCR ADIKCGSQAG 

       130        140        150        160        170        180 
GKLCPNNLCC SQWGFCGLGS EFCGGGCQSG ACSTDKPCGK DAGGRVCTNN YCCSKWGSCG 

       190        200        210 
IGPGYCGAGC QSGGCDGVFA EAITANSTLL QE 

« Hide

References

[1]"Nucleotide sequences of cDNA clones encoding wheat germ agglutinin isolectins A and D."
Smith J.J., Raikhel N.V.
Plant Mol. Biol. 13:601-603(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence variability in three wheat germ agglutinin isolectins: products of multiple genes in polyploid wheat."
Wright C.S., Raikhel N.V.
J. Mol. Evol. 28:327-336(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-197.
Tissue: Germ.
[3]"Comparison of the refined crystal structures of two wheat germ isolectins."
Wright C.S.
J. Mol. Biol. 209:475-487(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-197, PYROGLUTAMATE FORMATION AT GLN-27.
[4]"2.2-A resolution structure analysis of two refined N-acetylneuraminyl-lactose-wheat germ agglutinin isolectin complexes."
Wright C.S.
J. Mol. Biol. 215:635-651(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH N-ACETYLNEURAMINYL-LACTOSE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M25536 mRNA. Translation: AAA34256.1.
PIRS09623.
UniGeneTa.12645.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGCX-ray2.20A/B28-197[»]
2CWGX-ray2.00A/B28-197[»]
2UVOX-ray1.40A/B/E/F28-197[»]
2X3TX-ray2.75A/B/C/D28-197[»]
4AMLX-ray1.60A/B28-197[»]
7WGAX-ray2.00A/B28-197[»]
ProteinModelPortalP10968.
SMRP10968. Positions 27-197.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome3501. Tri a 18.0101.
650. Tri a 18.
CAZyCBM18. Carbohydrate-Binding Module Family 18.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsTraes_1AL_B8B0A092C.1; Traes_1AL_B8B0A092C.1; Traes_1AL_B8B0A092C.

Organism-specific databases

GrameneP10968.

Family and domain databases

Gene3D3.30.60.10. 4 hits.
InterProIPR001002. Chitin-bd_1.
IPR018371. Chitin-binding_1_CS.
[Graphical view]
PfamPF00187. Chitin_bind_1. 4 hits.
[Graphical view]
PRINTSPR00451. CHITINBINDNG.
ProDomPD000609. Chitin_bd_1. 3 hits.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00270. ChtBD1. 4 hits.
[Graphical view]
SUPFAMSSF57016. SSF57016. 4 hits.
PROSITEPS00026. CHIT_BIND_I_1. 4 hits.
PS50941. CHIT_BIND_I_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP10968.
PROP10968.

Entry information

Entry nameAGI1_WHEAT
AccessionPrimary (citable) accession number: P10968
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1990
Last modified: April 16, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references